RU2010138610A - STABILIZATION OF DEHYDROGENASES BY STABLE COFERENCES - Google Patents
STABILIZATION OF DEHYDROGENASES BY STABLE COFERENCES Download PDFInfo
- Publication number
- RU2010138610A RU2010138610A RU2010138610/10A RU2010138610A RU2010138610A RU 2010138610 A RU2010138610 A RU 2010138610A RU 2010138610/10 A RU2010138610/10 A RU 2010138610/10A RU 2010138610 A RU2010138610 A RU 2010138610A RU 2010138610 A RU2010138610 A RU 2010138610A
- Authority
- RU
- Russia
- Prior art keywords
- dehydrogenase
- enzyme
- independently
- case
- stable coenzyme
- Prior art date
Links
- 108020005199 Dehydrogenases Proteins 0.000 title claims abstract 3
- 230000006641 stabilisation Effects 0.000 title claims abstract 3
- 238000011105 stabilization Methods 0.000 title claims abstract 3
- 238000000034 method Methods 0.000 claims abstract 28
- 108090000790 Enzymes Proteins 0.000 claims abstract 21
- 102000004190 Enzymes Human genes 0.000 claims abstract 21
- 239000005515 coenzyme Substances 0.000 claims abstract 15
- 150000001875 compounds Chemical class 0.000 claims abstract 9
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 claims abstract 7
- 229910052760 oxygen Inorganic materials 0.000 claims abstract 7
- 229910052717 sulfur Inorganic materials 0.000 claims abstract 7
- 101710088194 Dehydrogenase Proteins 0.000 claims abstract 6
- XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 claims abstract 6
- 125000004122 cyclic group Chemical group 0.000 claims abstract 6
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims abstract 6
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 claims abstract 5
- 229950006238 nadide Drugs 0.000 claims abstract 5
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims abstract 4
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 claims abstract 4
- 108010050201 2-hydroxybutyrate dehydrogenase Proteins 0.000 claims abstract 2
- 229930024421 Adenine Natural products 0.000 claims abstract 2
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 claims abstract 2
- 108010021809 Alcohol dehydrogenase Proteins 0.000 claims abstract 2
- 102000007698 Alcohol dehydrogenase Human genes 0.000 claims abstract 2
- 108010009384 L-Iditol 2-Dehydrogenase Proteins 0.000 claims abstract 2
- 108030000198 L-amino-acid dehydrogenases Proteins 0.000 claims abstract 2
- 102000003855 L-lactate dehydrogenase Human genes 0.000 claims abstract 2
- 108700023483 L-lactate dehydrogenases Proteins 0.000 claims abstract 2
- 108010026217 Malate Dehydrogenase Proteins 0.000 claims abstract 2
- 102000013460 Malate Dehydrogenase Human genes 0.000 claims abstract 2
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical group C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 claims abstract 2
- 102100026974 Sorbitol dehydrogenase Human genes 0.000 claims abstract 2
- 229960000643 adenine Drugs 0.000 claims abstract 2
- 150000001413 amino acids Chemical class 0.000 claims abstract 2
- 235000011187 glycerol Nutrition 0.000 claims abstract 2
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 claims abstract 2
- 150000003839 salts Chemical class 0.000 claims abstract 2
- 125000004432 carbon atom Chemical group C* 0.000 claims 3
- 239000003153 chemical reaction reagent Substances 0.000 claims 3
- 229910052739 hydrogen Inorganic materials 0.000 claims 3
- 125000005842 heteroatom Chemical group 0.000 claims 2
- 229910052757 nitrogen Inorganic materials 0.000 claims 2
- GVNVAWHJIKLAGL-UHFFFAOYSA-N 2-(cyclohexen-1-yl)cyclohexan-1-one Chemical compound O=C1CCCCC1C1=CCCCC1 GVNVAWHJIKLAGL-UHFFFAOYSA-N 0.000 claims 1
- 101150065749 Churc1 gene Proteins 0.000 claims 1
- 102100038239 Protein Churchill Human genes 0.000 claims 1
- 125000000217 alkyl group Chemical group 0.000 claims 1
- 239000012491 analyte Substances 0.000 claims 1
- 229910052799 carbon Inorganic materials 0.000 claims 1
- 125000006297 carbonyl amino group Chemical group [H]N([*:2])C([*:1])=O 0.000 claims 1
- 239000002274 desiccant Substances 0.000 claims 1
- 238000001514 detection method Methods 0.000 claims 1
- 238000001035 drying Methods 0.000 claims 1
- 230000002255 enzymatic effect Effects 0.000 claims 1
- 230000003301 hydrolyzing effect Effects 0.000 claims 1
- 239000007791 liquid phase Substances 0.000 claims 1
- 239000000126 substance Substances 0.000 claims 1
- 125000001424 substituent group Chemical group 0.000 claims 1
- UUFQTNFCRMXOAE-UHFFFAOYSA-N 1-methylmethylene Chemical compound C[CH] UUFQTNFCRMXOAE-UHFFFAOYSA-N 0.000 abstract 1
- 101100167062 Caenorhabditis elegans chch-3 gene Proteins 0.000 abstract 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0014—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4)
- C12N9/0016—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4) with NAD or NADP as acceptor (1.4.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01001—Alcohol dehydrogenase (1.1.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01006—Glycerol dehydrogenase (1.1.1.6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01027—L-Lactate dehydrogenase (1.1.1.27)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01028—D-Lactate dehydrogenase (1.1.1.28)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01037—Malate dehydrogenase (1.1.1.37)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01047—Glucose 1-dehydrogenase (1.1.1.47)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y104/00—Oxidoreductases acting on the CH-NH2 group of donors (1.4)
- C12Y104/01—Oxidoreductases acting on the CH-NH2 group of donors (1.4) with NAD+ or NADP+ as acceptor (1.4.1)
- C12Y104/01005—L-Amino-acid dehydrogenase (1.4.1.5)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
1. Способ стабилизации фермента, отличающийся тем, что фермент хранят в присутствии стабильного кофермента. ! 2. Способ по п.1, отличающийся тем, что фермент выбран из дегидрогеназ. ! 3. Способ по п.2, отличающийся тем, что фермент представляет собой дегидрогеназу, выбранную из глюкозодегидрогеназы (Е.С.1.1.1.47), лактатдегидрогеназы (Е.С.1.1.1.27, 1.1.1.28), малатдегидрогеназы (Е.С.1.1.1.37), глицериндегидрогеназы (Е.С.1.1.1.6), алкогольдегидрогеназы (Е.С.1.1.1.1), альфа-гидроксибутиратдегидрогеназы, сорбитдегидрогеназы или дегидрогеназы аминокислоты, например дегидрогеназы L-аминокислоты (Е.С.1.4.1.5). ! 4. Способ по любому из пп.1-3, отличающийся тем, что в качестве фермента используют глюкозодегидрогеназу. ! 5. Способ по любому из пп.1-4, отличающийся тем, что стабильный кофермент выбран из стабильных соединений никотинамидадениндинуклеотида (NAD/NADH), и соединений никотинамидадениндинуклеотидфосфата (NADP/NADPH), и соединения формулы (I) ! ! 6. Способ по п.5, отличающийся тем, что стабильный кофермент выбран из соединений, имеющих общую формулу (II) ! ! в которой ! A=аденин или его аналог, ! T=в каждом случае независимо O, S, ! U=в каждом случае независимо OH, SH, BH3 -, BCNH2 -, ! V=в каждом случае независимо OH или фосфатная группа или две группы, образующие циклическую фосфатную группу; ! W=COOR, CON(R)2, COR, CSN(R)2, где R=в каждом случае независимо Н или С1-С2-алкил, ! Х2, Х2=в каждом случае независимо О, СН2, СНСН3, С(СН3)2, NH, NCH3, ! Y=NH, S, O, CH2, ! Z=линейный или циклический органический радикал, при условии, что Z и пиридиновый остаток не связаны посредством гликозидной связи, или его соль, или, где целесообразно, его восстановленная форма. ! 7. Способ по п.6, в котором Z выбран из ! (i) линейного радик 1. The method of stabilization of the enzyme, characterized in that the enzyme is stored in the presence of a stable coenzyme. ! 2. The method according to claim 1, characterized in that the enzyme is selected from dehydrogenases. ! 3. The method according to claim 2, characterized in that the enzyme is a dehydrogenase selected from glucose dehydrogenase (E.C.1.1.1.47), lactate dehydrogenase (E.C.1.1.1.27, 1.1.1.28), malate dehydrogenase (E.C. .1.1.1.37), glycerin dehydrogenase (E.C.1.1.1.6), alcohol dehydrogenase (E.C.1.1.1.1), alpha-hydroxybutyrate dehydrogenase, sorbitol dehydrogenase or amino acid dehydrogenase, e.g. L-amino acid dehydrogenase (E.C.1.4.1.5 ) ! 4. The method according to any one of claims 1 to 3, characterized in that glucose dehydrogenase is used as the enzyme. ! 5. The method according to any one of claims 1 to 4, characterized in that the stable coenzyme is selected from stable compounds of nicotinamide adenine dinucleotide (NAD / NADH), and compounds of nicotinamide adenine dinucleotide phosphate (NADP / NADPH), and a compound of formula (I)! ! 6. The method according to claim 5, characterized in that the stable coenzyme is selected from compounds having the general formula (II)! ! wherein ! A = adenine or its analog,! T = in each case, independently O, S,! U = in each case independently OH, SH, BH3 -, BCNH2 -,! V = in each case, independently OH or a phosphate group or two groups forming a cyclic phosphate group; ! W = COOR, CON (R) 2, COR, CSN (R) 2, where R = in each case independently H or C1-C2-alkyl,! X2, X2 = in each case, independently O, CH2, CHCH3, C (CH3) 2, NH, NCH3,! Y = NH, S, O, CH2,! Z = a linear or cyclic organic radical, provided that Z and the pyridine residue are not linked via a glycosidic bond, or a salt thereof, or, where appropriate, its reduced form. ! 7. The method according to claim 6, in which Z is selected from! (i) linear radic
Claims (24)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP08003054.7 | 2008-02-19 | ||
| EP08003054A EP2093284A1 (en) | 2008-02-19 | 2008-02-19 | Stabilisation of dehydrogenases with stable coenzymes |
| PCT/EP2009/001206 WO2009103540A1 (en) | 2008-02-19 | 2009-02-19 | Stabilization of dehydrogenases using stable coenzymes |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| RU2010138610A true RU2010138610A (en) | 2012-03-27 |
| RU2499834C2 RU2499834C2 (en) | 2013-11-27 |
Family
ID=39768713
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2010138610/10A RU2499834C2 (en) | 2008-02-19 | 2009-02-19 | Stabilisation of dehydrogenases with stable coferments |
Country Status (15)
| Country | Link |
|---|---|
| US (2) | US9896666B2 (en) |
| EP (2) | EP2093284A1 (en) |
| JP (2) | JP5758128B2 (en) |
| KR (3) | KR20130081300A (en) |
| CN (3) | CN104450659A (en) |
| AR (1) | AR070436A1 (en) |
| AU (1) | AU2009216908B9 (en) |
| BR (1) | BRPI0907839A2 (en) |
| CA (1) | CA2721718C (en) |
| HK (1) | HK1208703A1 (en) |
| MX (1) | MX2010008920A (en) |
| RU (1) | RU2499834C2 (en) |
| TW (1) | TWI482860B (en) |
| WO (1) | WO2009103540A1 (en) |
| ZA (1) | ZA201006638B (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2652888C2 (en) * | 2012-11-02 | 2018-05-03 | Ф. Хоффманн-Ля Рош Аг | Reagent materials and associated test elements |
Families Citing this family (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7553615B2 (en) * | 2005-07-28 | 2009-06-30 | Roche Diagnostics Operations, Inc. | Compounds, methods, complexes, apparatuses and uses relating to stabile forms of NAD/NADH |
| EP2093284A1 (en) | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisation of dehydrogenases with stable coenzymes |
| EP2398909B1 (en) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Fast reaction kinetics of enzymes having low activity in dry chemistry layers |
| EP2226008A1 (en) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Method for producing an analytical magazine |
| EP2226007A1 (en) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Test element magazine with covered test fields |
| WO2010094427A2 (en) | 2009-02-19 | 2010-08-26 | Roche Diagnostics Gmbh | Compact storage of auxiliary analytical devices in a cartridge |
| KR20130127555A (en) * | 2009-02-19 | 2013-11-22 | 에프. 호프만-라 로슈 아게 | Fast reaction kinetics of enzymes having low activity in dry chemistry layers |
| EP2292751A1 (en) * | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisation of enzymes with stable coenzymes |
| WO2011073258A1 (en) * | 2009-12-16 | 2011-06-23 | F. Hoffmann-La Roche Ag | Detecting the decomposition of enzymes in a test element by means of controlled release of protected analyte |
| EP2636750A1 (en) * | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
| SG11201407668XA (en) | 2012-06-22 | 2015-01-29 | Hoffmann La Roche | Method and device for detecting an analyte in a body fluid |
| US8920628B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Systems and methods for multiple analyte analysis |
| CN104854457B (en) | 2012-12-20 | 2016-09-14 | 霍夫曼-拉罗奇有限公司 | Method for analyzing body fluid samples |
| PL2936124T3 (en) | 2012-12-20 | 2017-08-31 | F.Hoffmann-La Roche Ag | Methods for evaluating medical measurement curves |
| EP2781919A1 (en) | 2013-03-19 | 2014-09-24 | Roche Diagniostics GmbH | Method / device for generating a corrected value of an analyte concentration in a sample of a body fluid |
| WO2014180939A1 (en) | 2013-05-08 | 2014-11-13 | Roche Diagnostics Gmbh | Stabilization of enzymes by nicotinic acid |
| WO2014195363A1 (en) * | 2013-06-04 | 2014-12-11 | Roche Diagnostics Gmbh | Novel compounds useful for fret and methods related thereto |
| WO2015063025A1 (en) | 2013-10-29 | 2015-05-07 | F. Hoffmann-La Roche Ag | Nano-enzyme containers for test elements |
| WO2015078899A1 (en) | 2013-11-27 | 2015-06-04 | Roche Diagnostics Gmbh | Composition comprising up-converting phosphors for detecting an analyte |
| EP2927319A1 (en) | 2014-03-31 | 2015-10-07 | Roche Diagnostics GmbH | High load enzyme immobilization by crosslinking |
| CN106164054B (en) | 2014-04-14 | 2019-05-07 | 豪夫迈·罗氏有限公司 | phenazine mediator |
| CN111848578B (en) | 2014-08-22 | 2023-10-31 | 豪夫迈·罗氏有限公司 | redox indicator |
| CN107779459B (en) * | 2016-08-31 | 2021-06-08 | 安琪酵母股份有限公司 | Glucose dehydrogenase DNA molecule, vector, strain and application |
| PL3523639T3 (en) | 2016-10-05 | 2025-03-17 | F. Hoffmann-La Roche Ag | Detection reagents and electrode arrangements for multi-analyte diagnostic test elements, as well as methods of using the same |
| EP3339431A1 (en) | 2016-12-22 | 2018-06-27 | Roche Diabetes Care GmbH | Glucose dehydrogenase variants with improved properties |
| WO2019166394A1 (en) | 2018-02-28 | 2019-09-06 | F. Hoffmann-La Roche Ag | Biocompatibility coating for continuous analyte measurement |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU1043568A1 (en) * | 1981-06-11 | 1983-09-23 | Московский Ордена Ленина,Ордена Октябрьской Революции И Ордена Трудового Красного Знамени Государственный Университет Им.М.В.Ломоносова | Blood dehydrogenase activity determination method |
| DE19543493A1 (en) * | 1995-11-22 | 1997-05-28 | Boehringer Mannheim Gmbh | Stabilized coenzyme solutions and their use for the determination of dehydrogenases or their substrates in an alkaline environment |
| US5801006A (en) | 1997-02-04 | 1998-09-01 | Specialty Assays, Inc. | Use of NADPH and NADH analogs in the measurement of enzyme activities and metabolites |
| US6380380B1 (en) | 1999-01-04 | 2002-04-30 | Specialty Assays, Inc. | Use of nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucliotide phosphate (NADP) analogs to measure enzyme activities metabolites and substrates |
| WO2001094370A1 (en) | 2000-06-07 | 2001-12-13 | Wako Pure Chemical Industries, Ltd. | Coenzyme derivatives and enzymes appropriate therefor |
| WO2002036779A1 (en) * | 2000-10-31 | 2002-05-10 | Koji Sode | Novel glucose dehydrogenase and process for producing the dehydrogenase |
| JP2003310274A (en) * | 2002-04-30 | 2003-11-05 | Amano Enzyme Inc | Glucose dehydrogenase and gene encoding the same |
| BR0309947B1 (en) | 2002-05-16 | 2013-11-26 | Process and device for producing polymer layers on transparent support, their use and process for producing a sensor | |
| MXPA06001719A (en) * | 2003-08-11 | 2006-05-19 | Codexis Inc | Improved glucose dehydrogenase polypeptides and related polynucleotides. |
| ES2541680T3 (en) | 2004-03-06 | 2015-07-23 | F. Hoffmann-La Roche Ag | Body fluid sampling device |
| US7172890B2 (en) * | 2004-10-28 | 2007-02-06 | Roche Diagnostics Gmbh | Inactivated enzyme variants and associated process and reagent system |
| US7553615B2 (en) | 2005-07-28 | 2009-06-30 | Roche Diagnostics Operations, Inc. | Compounds, methods, complexes, apparatuses and uses relating to stabile forms of NAD/NADH |
| DE102005035461A1 (en) * | 2005-07-28 | 2007-02-15 | Roche Diagnostics Gmbh | Stable NAD / NADH derivatives |
| EP2093284A1 (en) * | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisation of dehydrogenases with stable coenzymes |
| US20110313009A1 (en) | 2008-07-17 | 2011-12-22 | Horizon Pharma Usa, Inc. | Nsaid dose unit formulations with h2-receptor antagonists and methods of use |
| EP2398909B1 (en) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Fast reaction kinetics of enzymes having low activity in dry chemistry layers |
-
2008
- 2008-02-19 EP EP08003054A patent/EP2093284A1/en not_active Ceased
-
2009
- 2009-02-18 TW TW098105120A patent/TWI482860B/en not_active IP Right Cessation
- 2009-02-19 BR BRPI0907839-8A patent/BRPI0907839A2/en not_active Application Discontinuation
- 2009-02-19 KR KR1020137013118A patent/KR20130081300A/en not_active Withdrawn
- 2009-02-19 RU RU2010138610/10A patent/RU2499834C2/en not_active IP Right Cessation
- 2009-02-19 AU AU2009216908A patent/AU2009216908B9/en not_active Revoked
- 2009-02-19 JP JP2010547110A patent/JP5758128B2/en not_active Expired - Fee Related
- 2009-02-19 AR ARP090100571A patent/AR070436A1/en not_active Application Discontinuation
- 2009-02-19 KR KR1020107020894A patent/KR101381004B1/en not_active Expired - Fee Related
- 2009-02-19 CN CN201410680334.8A patent/CN104450659A/en active Pending
- 2009-02-19 CN CN200980105640.6A patent/CN101945999B/en not_active Expired - Fee Related
- 2009-02-19 CA CA2721718A patent/CA2721718C/en not_active Expired - Fee Related
- 2009-02-19 WO PCT/EP2009/001206 patent/WO2009103540A1/en not_active Ceased
- 2009-02-19 KR KR1020127027270A patent/KR20120134142A/en not_active Ceased
- 2009-02-19 MX MX2010008920A patent/MX2010008920A/en active IP Right Grant
- 2009-02-19 EP EP09712033.1A patent/EP2245152B1/en active Active
-
2010
- 2010-02-12 JP JP2011550531A patent/JP6113405B2/en not_active Expired - Fee Related
- 2010-02-12 CN CN2010800085457A patent/CN102325896A/en active Pending
- 2010-08-19 US US12/859,654 patent/US9896666B2/en active Active
- 2010-09-16 ZA ZA2010/06638A patent/ZA201006638B/en unknown
-
2015
- 2015-09-23 HK HK15109305.4A patent/HK1208703A1/en unknown
-
2018
- 2018-01-11 US US15/868,055 patent/US11220674B2/en active Active
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2652888C2 (en) * | 2012-11-02 | 2018-05-03 | Ф. Хоффманн-Ля Рош Аг | Reagent materials and associated test elements |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2010138610A (en) | STABILIZATION OF DEHYDROGENASES BY STABLE COFERENCES | |
| JP2011514153A5 (en) | ||
| RU2015120693A (en) | REAGENT MATERIALS AND RELATED TEST ELEMENTS | |
| CA2614792A1 (en) | Stable nad/nadh derivatives | |
| JP5851401B2 (en) | Enzyme stabilization with stable coenzymes | |
| JP2013502212A5 (en) | ||
| JP2012517816A5 (en) | ||
| JP2009502844A5 (en) | ||
| JP2015511820A5 (en) | ||
| AU2012203453B2 (en) | Stabilization of dehydrogenases using stable coenzymes | |
| Pretorius et al. | Deuterium isotope effects for the oxidation of 1-methyl-3-phenyl-3-pyrrolinyl analogues by monoamine oxidase B | |
| JP2022037877A (en) | Sensitizer in superoxide anion detection system | |
| Song et al. | Simple Preparation of Diaphorase/Polysiloxane Viologen Polymer Modified Electrode for Sensing NAD and NADH | |
| HK1152728B (en) | Stabilization of dehydrogenases using stable coenzymes |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | The patent is invalid due to non-payment of fees |
Effective date: 20170220 |